Analytical Data
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Gene name
HLA-C*03:04&B2M&KRAS G12D(GADGVGKSAL) Monomer
- Application
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Alternative Names
MHC; KRAS; K-Ras 2; KRAS2; C-K-RAS; CFC2; K-RAS2A; K-RAS2B; K-RAS4A; K-RAS4B; KRAS1; KRAS2; NS; NS3; RASK2; GTPase Kras; KI-RAS; RALD
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Species
Human
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Source
HEK293
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Tag
C-Avi;C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
QAV56463.1 (G25-T305)&P61769
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Expression Region
QAV56463.1 (G25-T305)&P61769 (I21-M119)&GADGVGKSAL
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Molecular Weight
55-65 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The study of the HLA-C*03:04/B2M/KRAS G12D (GADGVGKSAL) monomeric recombinant protein is pivotal in understanding immune responses against cancer, particularly in the context of Kras-driven tumors. KRAS mutations, such as G12D, are prevalent in various malignancies, including pancreatic and colorectal cancers, and are associated with poor prognosis. The peptide GADGVGKSAL derived from the KRAS G12D mutation is recognized by specific T cells, offering a unique opportunity to develop targeted immunotherapies. By investigating the HLA-C*03:04 molecule, which presents this mutant peptide on the cell surface, researchers can gain insights into how the immune system recognizes and responds to tumor-specific antigens. The recombinant protein serves as a model to study peptide binding affinity, T cell receptor interactions, and overall immune evasion mechanisms employed by tumors. This research could contribute to the design of personalized cancer vaccines and adoptive T cell therapies, harnessing the body’s immune system to target and eliminate cancer cells with KRAS mutations. Understanding the structure, function, and immunogenicity of the HLA-C*03:04/B2M/KRAS G12D complex not only enhances our comprehension of tumor immunology but also paves the way for innovative therapeutic strategies against resistant cancer types.
